ID A0A1L3ZR73_9SPHN Unreviewed; 130 AA.
AC A0A1L3ZR73;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=L-ectoine synthase {ECO:0000256|ARBA:ARBA00019707, ECO:0000256|HAMAP-Rule:MF_01255};
DE EC=4.2.1.108 {ECO:0000256|ARBA:ARBA00013192, ECO:0000256|HAMAP-Rule:MF_01255};
DE AltName: Full=N-acetyldiaminobutyrate dehydratase {ECO:0000256|ARBA:ARBA00033271, ECO:0000256|HAMAP-Rule:MF_01255};
GN Name=ectC {ECO:0000256|HAMAP-Rule:MF_01255};
GN ORFNames=BSL82_01420 {ECO:0000313|EMBL:API58124.1};
OS Tardibacter chloracetimidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Tardibacter.
OX NCBI_TaxID=1921510 {ECO:0000313|EMBL:API58124.1, ECO:0000313|Proteomes:UP000182063};
RN [1] {ECO:0000313|Proteomes:UP000182063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-A5 {ECO:0000313|Proteomes:UP000182063};
RA Lee H., Ka J.-O.;
RT "Complete Genome Sequence of alachlor-degrading Sphingomonas sp. strain JJ-
RT A5.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-
CC diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-
CC pyrimidine carboxylic acid), which is an excellent osmoprotectant.
CC {ECO:0000256|HAMAP-Rule:MF_01255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine;
CC Xref=Rhea:RHEA:17281, ChEBI:CHEBI:15377, ChEBI:CHEBI:58515,
CC ChEBI:CHEBI:58929; EC=4.2.1.108;
CC Evidence={ECO:0000256|ARBA:ARBA00000511, ECO:0000256|HAMAP-
CC Rule:MF_01255};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005181, ECO:0000256|HAMAP-Rule:MF_01255}.
CC -!- SIMILARITY: Belongs to the ectoine synthase family.
CC {ECO:0000256|ARBA:ARBA00009637, ECO:0000256|HAMAP-Rule:MF_01255}.
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DR EMBL; CP018221; API58124.1; -; Genomic_DNA.
DR RefSeq; WP_072595700.1; NZ_CP018221.1.
DR AlphaFoldDB; A0A1L3ZR73; -.
DR STRING; 1921510.BSL82_01420; -.
DR KEGG; sphj:BSL82_01420; -.
DR OrthoDB; 9801830at2; -.
DR UniPathway; UPA00067; UER00123.
DR Proteomes; UP000182063; Chromosome.
DR GO; GO:0033990; F:ectoine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06978; cupin_EctC; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR HAMAP; MF_01255; Ectoine_synth; 1.
DR InterPro; IPR010462; Ectoine_synth.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR39289; -; 1.
DR PANTHER; PTHR39289:SF1; L-ECTOINE SYNTHASE; 1.
DR Pfam; PF06339; Ectoine_synth; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01255};
KW Reference proteome {ECO:0000313|Proteomes:UP000182063}.
SQ SEQUENCE 130 AA; 14306 MW; 6505955A87F8EAB1 CRC64;
MLIRKLEEIR GTDRSVSDKG WESSRMLLAE DGMGFSFHIT TLQAGGEWTF HYQHHVESVF
VISGRGSVED LATGERHELA PGTLYALNAH DRHTLRAETE LVTACVFNPP VTGNEVHDET
GAYRPAAAAA
//